Introduction to biological molecules Flashcards

1
Q

Explain Ionic bonding?

A

Ionic bonding is the gain and loss of electrons between a metal and non-metal atom joining to have an increased stability

Ionic bonds are joined together by very weal electrostatic interactions, making them very double in water

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2
Q

Why is maintaining the ion concentration critical?

A

Maintaining the ion concentration is critical as the cell must be able to maintain a balance of ion charge difference. If this is lost the cell can become turgid and burst or flaccid and die

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3
Q

Give features of covalent bonds

A

Covalent bonds;

  • Electrons are being shared
  • Can be one from each atom or more
  • Stronger than an ionic bond
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4
Q

Give features of polar bonds?

A

Polar bonds;
- Not all electrons are shared equally which creates a slightly positive and negative side allowing for electrostatic interactions

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5
Q

Give features of hydrogen bonding ?

A

Hydrogen bonding;
Hydrogen is slightly charged and attracted to molecules that are slightly negatively charged, creating a weak intermolecular force of attraction.

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6
Q

Give features of Van Der Waals forces?

A

Vander waals forces;

  • Very weak interaction
  • Relatively transient (last for a short period of time)
  • They determine how close individual atoms can get to one another, determining the overall 3D shape of a molecule
  • The nucleus is surrounded by electrons that are constantly cycling, however they can have more electrons on one side than the other creating a negative charge. Causing neighbouring atoms to repel or attract.
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7
Q

Give some intermolecular bonding?

A
  • Disulphide bridge
  • Hydrogen bonding
  • Hydrophobic interactions
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8
Q

What is the general structure for sugars?

A

(CH2O)n - 1 Carbon, 2 Hydrogen and 1 Oxygen

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9
Q

What is the function of sugar within a cell?

A

Sugar is a source of energy for a cell

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10
Q

Why can’t the same enzyme breakdown both glucose and galactose?

A

Enzymes can detect small differences in structures

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11
Q

What is sugar a form of?

A

Sugar is a form of carbohydrate

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12
Q

What is it called when 2 different sugars are joined together?

A

When 2 different sugars are joined together they are referred to as a Disaccharide molecule

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13
Q

Why might sugars be joined together?

A

Sugars can be joined together in long chains for storage to be consumed later when sugar is required

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14
Q

what are 1-2% of our muscles made. from?

A

1-2% of our muscles are made of glycogen for readily use of glucose

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15
Q

what is 5-6% of the liver composed of?

A

5-6% of the liver is composed of glycogen, causing the body to have a high supply of glucose on standby if any muscles in the body suddenly require it

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16
Q

What are fatty acids made from?

A

Fatty acids are made from hydrocarbon chains (A chain head and a long hydrogen and carbon tail)

17
Q

What kind of charge does the head of the hydrocarbon chain have?

A

The head of the hydro carbon chain as a negative charge because it is a carbide group (hydrophilic)

18
Q

How can fatty acids be stored?

A

Fatty acids can be stored as triacyl glycerol which can be used as a source of energy

19
Q

What can triacyl glycerol be broken down into and what can that substance be further broken down into as used for?

A

Triacyl glycerol can be broken down into fatty acids, which can then be broken down into acetyl coA which can be used in the citric acid cycle.

Fatty acids can also be broken down into glycerol which can be converted to make glucose and used to make energy through glycolysis.

20
Q

How are fatty acids used in cells?

A

Fatty acids are very important components of cell membranes, they can be linked onto a head chain act as the hydrophobic tail of a cell membrane. The hydrophobic and hydrophilic properties of these hydrocarbon chains allows the lipid bilayer membrane to be created

21
Q

What are the features of steroids?

A

Steroids;

  • Are rich in carbon and hydrogen
  • 4 fused carbon rings. with different functional groups attached
  • Made in the body (e.g cholesterol - high cholesterol means that. there is too much of the steroid cholesterol) - statins are used to inhibit the pathways that synthesises steroids like cholestrol
22
Q

Draw an amino acid?

A

Amino acids have a core central carbon atom which on one side has an amino group (a nitrogen and some hydrogens, one hydrogen is positively charged making that functional group acidic) and on the other side they have a carboxyl group (carbon with one double bond to an oxygen and one single bond to an oxygen, making that group basic). They have an R-group which determines the type of amino acid.

23
Q

What can amino acids be polymerised together with?

A

Amino acids can be polymerised together via a peptide bond to make a protein

24
Q

Explain the chemistry behind a peptide bond?

A

In a peptide bond the negatively charged carboxide group of one amino acid reacts with the adjacent amino group of another amino acid where the carbon becomes joined to the
nitrogen.

25
Q

What are the 2 ends of amino acids that have been joined together called?

A

The end which has the free amino group is referred to as the N-Terminus and the end which has the free carboxide group is referred to as being the C-Terminus

26
Q

What are the 3 uses of amino acids?

A

Amino acids

  • Sources of energy
  • Neurotransmitters - E.g - Glutamic acid
  • Precursors for other molecules (used to make other molecules).

E.g - Glycine is a precursor for porphyrin ring which is amino acids joined to an iron atom

27
Q

What is the structure of a Nucleotide ?

A

Nucleotides have a carbon - nitrogen ring (base) linked onto a five carbon sugar, where the sugar can be ribose (RNA) or Deoxyribose (DNA). It also has phosphate groups attached to the sugar (usually 3 and 1 is taken off to make ATP).

28
Q

What is the role of nucleotides?

A

Nucleotides are short term energy stores - ATP and GTP

Nucleotides can store electrons - NAD, NADP reducing store for biosynthesis of ATP reduction

29
Q

What is a cofactor?

A

A cofactor is a non-protein part of an enzyme that is required for biological activity of that enzyme, like a helper molecule.

E.g - Cyclic AMP is used in signalling to activate enzymes

30
Q

Give 2 examples of biomolecules that are hybrids?

A

Glycoprotein - Protein bound to lots of sugars

Glycolipid - A lipid bound to sugars

31
Q

What does the addition of sugars to biomolecules allow?

A

The addition of sugars can help stabilise the protein or lipid

32
Q

What is peptidoglycans and where are they found ?

A

Peptidoglycans are found in bacteria wall, have a short peptide chain and very long sugars.

33
Q

What are proteoglycans?

A

Proteoglycans are proteins from the extracellular matrix which have lots of sugars

34
Q

How does the structure of proteins influence immune response ?

A
  • The difference between blood groups A, B and O is due to the different sugars that are present on lipids that are buried in the surface of the red blood cell.
  • The outside coat of viruses are surrounded by loads of glycoproteins / sugars
35
Q

How do glycoproteins affect vaccines?

A

The sequence of sugars becomes an issue when giving vaccines as the Glycoproteins that are on the surface of the virus bind to the receptors in order to gain access to the human cell. Vaccinations try to block these interactions, however viruses can change the nature. of their sugar on the outside as they aren’t determined by genetic codes

36
Q

What can changes in amino acids result in?

A

A change in one amino acid can alter the receptors on an enzyme, meaning the protein cannot work properly as the binding site is not as robust

37
Q

What can changes in DNA lead to ?

A

Changes in DNA structures can prelude to mutations which can cause issues like cancers